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SALTY:PEPE
Contents
Species (Taxon ID) | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). (99287) | |
Gene Name(s) | pepE | |
Protein Name(s) | Peptidase E
Alpha-aspartyl dipeptidase Asp-specific dipeptidase Dipeptidase E | |
External Links | ||
UniProt | P36936 | |
EMBL | U01246 AE006468 | |
PIR | A36867 | |
RefSeq | NP_463055.1 | |
PDB | 1FY2 1FYE | |
PDBsum | 1FY2 1FYE | |
ProteinModelPortal | P36936 | |
SMR | P36936 | |
STRING | 99287.STM4190 | |
MEROPS | S51.001 | |
PRIDE | P36936 | |
EnsemblBacteria | AAL23014 | |
GeneID | 1255716 | |
KEGG | stm:STM4190 | |
PATRIC | 32387273 | |
HOGENOM | HOG000281834 | |
KO | K05995 | |
OMA | TPYIGWS | |
OrthoDB | EOG6M6JST | |
PhylomeDB | P36936 | |
BioCyc | SENT99287:GCTI-4220-MONOMER | |
EvolutionaryTrace | P36936 | |
Proteomes | UP000001014 | |
GO | GO:0005737 GO:0016805 GO:0008236 | |
Gene3D | 3.40.50.880 | |
HAMAP | MF_00510 | |
InterPro | IPR029062 IPR005320 IPR023172 | |
Pfam | PF03575 | |
SUPFAM | SSF52317 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0016805 |
dipeptidase activity |
ECO:0000314 |
F |
Table 4 shows that Peptidase E cleaved several types of dipeptides. It did cleave one type of tripeptide, but this is most likely because it is smallest aspartyl tripeptide. |
complete | |||||
GO:0016787 |
hydrolase activity |
ECO:0000315 |
F |
Figure 3 shows that none of the mutant phenotypes of peptidase E hydrolyze Asp-pNA as well as the wild type. |
complete | |||||
enables |
GO:0008233 |
peptidase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11920 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0006508 |
proteolysis |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0008236 |
serine-type peptidase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016805 |
dipeptidase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000103203 |
C |
Seeded From UniProt |
complete | ||
involved_in |
GO:0006508 |
proteolysis |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000103203 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0016805 |
dipeptidase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000103203 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0016805 |
dipeptidase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0008236 |
serine-type peptidase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006508 |
proteolysis |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0008233 |
peptidase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016787 |
hydrolase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Lassy, RA & Miller, CG (2000) Peptidase E, a peptidase specific for N-terminal aspartic dipeptides, is a serine hydrolase. J. Bacteriol. 182 2536-43 PubMed GONUTS page
- ↑ Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
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